Classifier Instance:

Anchor text: c-ring
Target Entity: ATP_synthase_subunit_C
Preceding Context: The crystal structure of the F 1 showed alternating alpha and beta subunits (3 of each), arranged like segments of an orange around an asymmetrical gamma subunit. According to the current model of ATP synthesis (known as the alternating catalytic model), the proton-motive force across the inner mitochondrial membrane, generated by the electron transport chain, drives the passage of protons through the membrane via the F O region of ATP synthase. A portion of the F O (the ring of c-subunits) rotates as the protons pass through the membrane. The
Succeeding Context: is tightly attached to the asymmetric central stalk (consisting primarily of the gamma subunit), which rotates within the alpha 3 beta 3 of F 1 causing the 3 catalytic nucleotide binding sites to go through a series of conformational changes that leads to ATP synthesis. The major F 1 subunits are prevented from rotating in sympathy with the central stalk rotor by a peripheral stalk that joins the alpha 3 beta 3 to the non-rotating portion of F O . The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F 1 to F O . Under the right conditions, the enzyme reaction can also be carried out in reverse, with ATP hydrolysis driving proton pumping across the membrane.
Paragraph Title: Binding-change model
Source Page: ATP synthase

Ground Truth Types:

Predicted Types:

Type	Confidence	Decision
wordnet_artifact_100021939	-1.7668066775514177	0
wordnet_event_100029378	-1.2049744234618625	0
wordnet_organization_108008335	-2.3683559010866837	0
wordnet_person_100007846	-2.5608185690664182	0
yagoGeoEntity	-1.8565835355881544	0